Urszula Derewenda

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Primary Appointment

Assistant Professor of Research, Molecular Physiology and Biological Physics

Research Interests

Our primary interest is in the mechanisms by which protein molecules accomplish their diverse biological tasks.

Research Description

Our primary interest is in the mechanisms by which protein molecules accomplish their diverse biological tasks. Crystallography and molecular biology are the primary tools with which we probe into the structure-function relationships in complex proteins. There are two major themes in our work: structural biology of cytoskeletal regulation and the mechanism of hydrolytic enzymes, such as esterases and thioesterases.

Personal Statement

Our primary interest is in the mechanisms by which protein molecules accomplish their diverse biological tasks. Crystallography and molecular biology are the primary tools with which we probe into the structure-function relationships in complex proteins. There are two major themes in our work: structural biology of cytoskeletal regulation and the mechanism of hydrolytic enzymes, such as esterases and thioesterases.

Selected Publications

2020

Derewenda, Z. S., Hawro, I., & Derewenda, U. (2020). C&x2500;HMIDLINE HORIZONTAL ELLIPSISO hydrogen bonds in kinase-inhibitor interfaces. IUBMB LIFE, 72(6), 1233-1242. doi:10.1002/iub.2282

2018

Radwanska, M. J., Jaskolowski, M., Davydova, E., Derewenda, U., Miyake, T., Engel, D. A., . . . Derewenda, Z. S. (2018). The structure of the C-terminal domain of the nucleoprotein from the Bundibugyo strain of the Ebola virus in complex with a pan-specific synthetic Fab. ACTA CRYSTALLOGRAPHICA SECTION D-STRUCTURAL BIOLOGY, 74, 681-689. doi:10.1107/S2059798318007878

Artamonov, M. V., Sonkusare, S. K., Good, M. E., Momotani, K., Eto, M., Isakson, B. E., . . . Somlyo, A. V. (2018). RSK2 contributes to myogenic vasoconstriction of resistance arteries by activating smooth muscle myosin and the Na+/H+ exchanger. SCIENCE SIGNALING, 11(554). doi:10.1126/scisignal.aar3924

2017

Bukrejewska, M., Derewenda, U., Radwanska, M., Engel, D. A., & Derewenda, Z. S. (2017). Crystal structures of the methyltransferase and helicase from the ZIKA 1947 MR766 Uganda strain. ACTA CRYSTALLOGRAPHICA SECTION D-STRUCTURAL BIOLOGY, 73, 767-774. doi:10.1107/S2059798317010737

2016

Utepbergenov, D., Hennig, P. M., Derewenda, U., Artamonov, M. V., Somlyo, A. V., & Derewenda, Z. S. (2016). Bacterial Expression, Purification and In Vitro Phosphorylation of Full-Length Ribosomal S6 Kinase 2 (RSK2). PLOS ONE, 11(10). doi:10.1371/journal.pone.0164343

Amin, E., Jaiswal, M., Derewenda, U., Reis, K., Nouri, K., Koessmeier, K. T., . . . Ahmadian, M. R. (2016). Deciphering the Molecular and Functional Basis of RHOGAP Family Proteins: A SYSTEMATIC APPROACH TOWARD SELECTIVE INACTIVATION OF RHO FAMILY PROTEINS. JOURNAL OF BIOLOGICAL CHEMISTRY, 291(39), 20353-20371. doi:10.1074/jbc.M116.736967

Baker, L. E., Ellena, J. F., Handing, K. B., Derewenda, U., Utepbergenov, D., Engel, D. A., & Derewenda, Z. S. (2016). Molecular architecture of the nucleoprotein C-terminal domain from the Ebola and Marburg viruses. ACTA CRYSTALLOGRAPHICA SECTION D-STRUCTURAL BIOLOGY, 72, 49-58. doi:10.1107/S2059798315021439

2014

Derewenda, Z., Dziubanska, P., Derewenda, U., Ellena, J., Haley, K., & Engel, D. (2014). The crystal structure of the C-terminal domain of the Ebola virus nucleoprotein. ACTA CRYSTALLOGRAPHICA A-FOUNDATION AND ADVANCES, 70, C1594. doi:10.1107/S2053273314084058

Dziubanska, P. J., Derewenda, U., Ellena, J. F., Engel, D. A., & Derewenda, Z. S. (2014). The structure of the C-terminal domain of the Zaire ebolavirus nucleoprotein. ACTA CRYSTALLOGRAPHICA SECTION D-STRUCTURAL BIOLOGY, 70, 2420-2429. doi:10.1107/S1399004714014710

2013

Artamonov, M. V., Momotani, K., Stevenson, A., Trentham, D. R., Derewenda, U., Derewenda, Z. S., . . . Somlyo, A. V. (2013). Agonist-induced Ca2+ Sensitization in Smooth Muscle REDUNDANCY OF RHO GUANINE NUCLEOTIDE EXCHANGE FACTORS (RhoGEFs) AND RESPONSE KINETICS, A CAGED COMPOUND STUDY. JOURNAL OF BIOLOGICAL CHEMISTRY, 288(47), 34030-34040. doi:10.1074/jbc.M113.514596

Yeh, T. -Y., Kowalska, A. K., Scipioni, B. R., Cheong, F. K. Y., Zheng, M., Derewenda, U., . . . Schroer, T. A. (2013). Dynactin helps target Polo-like kinase 1 to kinetochores via its left-handed beta-helical p27 subunit. EMBO JOURNAL, 32(7), 1023-1035. doi:10.1038/emboj.2013.30

Derewenda, U., Artamonov, M., Szukalska, G., Utepbergenov, D., Olekhnovich, N., Parikh, H. I., . . . Derewenda, Z. S. (2013). Identification of quercitrin as an inhibitor of the p90 S6 ribosomal kinase (RSK): structure of its complex with the N-terminal domain of RSK2 at 1.8 Ã resolution. ACTA CRYSTALLOGRAPHICA SECTION D-STRUCTURAL BIOLOGY, 69, 266-275. doi:10.1107/S0907444912045520

2012

Utepbergenov, D., Derewenda, U., Olekhnovich, N., Szukalska, G., Banerjee, B., Hilinski, M. K., . . . Derewenda, Z. S. (2012). Insights into the Inhibition of the p90 Ribosomal 56 Kinase (RSK) by the Flavonol Glycoside SL0101 from the 1.5 Ã Crystal Structure of the N-Terminal Domain of RSK2 with Bound Inhibitor. BIOCHEMISTRY, 51(33), 6499-6510. doi:10.1021/bi300620c

2011

Momotani, K., Artamonov, M. V., Utepbergenov, D., Derewenda, U., Derewenda, Z. S., & Somlyo, A. V. (2011). p63RhoGEF Couples Gαq/11-Mediated Signaling to Ca2+ Sensitization of Vascular Smooth Muscle Contractility. CIRCULATION RESEARCH, 109(9), 993-U42. doi:10.1161/CIRCRESAHA.111.248898

Zheng, M., Cierpicki, T., Burdette, A. J., Utepbergenov, D., Janczyk, P. L., Derewenda, U., . . . Derewenda, Z. S. (2011). Structural Features and Chaperone Activity of the NudC Protein Family. JOURNAL OF MOLECULAR BIOLOGY, 409(5), 722-741. doi:10.1016/j.jmb.2011.04.018

Kowalska, A. K., Zheng, M., Derewenda, U., & Derewenda, Z. S. (2011). The crystal structure of the p27 component of human dynactin. ACTA CRYSTALLOGRAPHICA A-FOUNDATION AND ADVANCES, 67, C222. doi:10.1107/S0108767311094463

Bielnicki, J. A., Shkumatov, A. V., Derewenda, U., Somlyo, A. V., Svergun, D. I., & Derewenda, Z. S. (2011). Insights into the Molecular Activation Mechanism of the RhoA-specific Guanine Nucleotide Exchange Factor, PDZRhoGEF. JOURNAL OF BIOLOGICAL CHEMISTRY, 286(40), 35163-35175. doi:10.1074/jbc.M111.270918

Zylkiewicz, E., Kijanska, M., Choi, W. -C., Derewenda, U., Derewenda, Z. S., & Stukenberg, P. T. (2011). The N-terminal coiled-coil of Ndell is a regulated scaffold that recruits LIS1 to dynein. JOURNAL OF CELL BIOLOGY, 192(3), 433-445. doi:10.1083/jcb.201011142